# Purification and characterization of polyphenol oxidase from cauliflower (Brassica oleracea L.)
> Rahman A.N.F.

URL kanonis: https://discover.unhas.ac.id/publications/pub_scopus_84859626173
Jurnal / Konferensi: Journal of Agricultural and Food Chemistry
Tahun terbit: 2012
DOI: https://doi.org/10.1021/jf300380b
ISSN: 00218561
Kuartil SJR: Q1
Citations: 21

## Authors
- Rahman A.N.F.

## Abstract
Polyphenol oxidase (PPO) of cauliflower was purified to 282-fold with a recovery rate of 8.1%, using phloroglucinol as a substrate. The enzyme appeared as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The estimated molecular weight of the enzyme was 60 and 54 kDa by SDS-PAGE and gel filtration, respectively. The purified enzyme, called phloroglucinol oxidase (PhO), oxidized phloroglucinol (K(m) = 3.3 mM) and phloroglucinolcarboxylic acid. The enzyme also had peroxidase (POD) activity. At the final step, the activity of purified cauliflower POD was 110-fold with a recovery rate of 3.2%. The PhO and POD showed the highest activity at pH 8.0 and 4.0 and were stable in the pH range of 3.0-11.0 and 5.0-8.0 at 5 °C for 20 h, respectively. The optimum temperature was 55 °C for PhO and 20 °C for POD. The most effective inhibitor for PhO was sodium diethyldithiocarbamate at 10 mM (IC(50) = 0.64 and K(i) = 0.15 mM), and the most effective inhibitor for POD was potassium cyanide at 1.0 mM (IC(50) = 0.03 and K(i) = 29 μM).

## Keywords
- Polyphenol oxidase
- Phloroglucinol
- Chemistry
- Peroxidase
- Sodium dodecyl sulfate
- Uncompetitive inhibitor
- Chromatography
- Gel electrophoresis
- Enzyme assay
- Polyacrylamide gel electrophoresis
- Potassium cyanide
- Sodium
- Biochemistry
- Polyphenol
- Point of delivery
- Sodium metabisulfite
- Enzyme
- Cyanide
- Non-competitive inhibition
- Antioxidant
- Food science
- Botany
- Organic chemistry
- Biology

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Sumber: Discover Unhas — RIMS Universitas Hasanuddin.
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